ID   GUNA_STRLI              Reviewed;         459 AA.
AC   P27035;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Endoglucanase CelA;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=celA;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-43.
RC   STRAIN=66 / 1326;
RX   PubMed=1575483; DOI=10.1128/aem.58.3.815-820.1992;
RA   Theberge M., Lacaze P., Shareck F., Morosoli R., Kluepfel D.;
RT   "Purification and characterization of an endoglucanase from Streptomyces
RT   lividans 66 and DNA sequence of the gene.";
RL   Appl. Environ. Microbiol. 58:815-820(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC   -!- PTM: The linker region (also termed 'hinge') may be a potential site
CC       for proteolysis.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; M82807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P27035; -.
DR   SMR; P27035; -.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.290; -; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR018366; CBM2_CS.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51173; CBM2; 1.
DR   PROSITE; PS00561; CBM2_A; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:1575483"
FT   CHAIN           28..459
FT                   /note="Endoglucanase CelA"
FT                   /id="PRO_0000007873"
FT   DOMAIN          28..134
FT                   /note="CBM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT   REGION          129..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..147
FT                   /note="Linker ('hinge') (Pro-Thr box)"
FT   REGION          148..357
FT                   /note="Catalytic"
FT   ACT_SITE        286
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   ACT_SITE        378
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O85465"
FT   DISULFID        31..131
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  48663 MW;  CFF47EC34E2F97A7 CRC64;
     MKRLLALLAT GVSIVGLTAL AGPPAQAATG CKAEYTITSQ WEGGFQAGVK ITNLGDPVSG
     WTLGFTMPDA GQRLVQGWNA TWSQSGSAVT AGGVDWNRTL ATGASADLGF VGSFTGANPA
     PTSFTLNGAT CSGSVTDPPT DPPTDPPATG TPAAVNGQLH VCGVHLCNQY DRPIQLRGMS
     THGIQWFGPC YGDASLDRLA QDWKSDLLRV AMYVQEDGYE TDPAGFTSRV NGLVDMAEDR
     GMYAVIDFHT LTPGDPNYNL DRARTFFSSV AARNDKKNVI YEIANEPNGV SWTAVKSYAE
     QVIPVIRAAD PDAVVIVGTR GWSSLGVSDG ANESEVVNNP VNATNIMYAF HFYAASHKDD
     YRAAVRPAAT RLPLFVSEFG TVSATAWSVD RSSSVAWLDL LDQLKISYAN WTYSDADEGS
     AAFRPGTCEG TDYSSSGVLT ESGALVKSRI STTDDFPTS